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ATG38_YEAST
ID   ATG38_YEAST             Reviewed;         226 AA.
AC   Q05789; D6VYL2;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 2.
DT   03-AUG-2022, entry version 137.
DE   RecName: Full=Autophagy-related protein 38 {ECO:0000303|PubMed:24165940};
GN   Name=ATG38 {ECO:0000303|PubMed:24165940};
GN   OrderedLocusNames=YLR211C {ECO:0000312|SGD:S000004201}; ORFNames=L8167.20;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169871;
RA   Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA   Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA   Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA   Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA   Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA   Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA   Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA   Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA   Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA   Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA   Zollner A., Hani J., Hoheisel J.D.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL   Nature 387:87-90(1997).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [3]
RP   REVISION OF GENE MODEL.
RX   PubMed=10734188; DOI=10.1093/nar/28.8.1700;
RA   Davis C.A., Grate L., Spingola M., Ares M. Jr.;
RT   "Test of intron predictions reveals novel splice sites, alternatively
RT   spliced mRNAs and new introns in meiotically regulated genes of yeast.";
RL   Nucleic Acids Res. 28:1700-1706(2000).
RN   [4]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [5]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE
RP   AUTOPHAGY-SPECIFIC VPS34 PI3-KINASE COMPLEX I, INTERACTION WITH ATG14 AND
RP   VPS34, SUBUNIT, SUBCELLULAR LOCATION, AND FUNCTION.
RX   PubMed=24165940; DOI=10.1083/jcb.201304123;
RA   Araki Y., Ku W.C., Akioka M., May A.I., Hayashi Y., Arisaka F.,
RA   Ishihama Y., Ohsumi Y.;
RT   "Atg38 is required for autophagy-specific phosphatidylinositol 3-kinase
RT   complex integrity.";
RL   J. Cell Biol. 203:299-313(2013).
CC   -!- FUNCTION: Autophagy-related protein required for cytoplasm to vacuole
CC       transport (Cvt) and autophagy as a part of the autophagy-specific VPS34
CC       PI3-kinase complex I. This complex is essential to recruit the ATG8-
CC       phosphatidylinositol conjugate and the ATG12-ATG5 conjugate to the pre-
CC       autophagosomal structure. ATG38 is required for the integrity of the
CC       active PI3-kinase complex I by maintaining an association between
CC       VPS15-VPS34 and ATG1P-VPS30 subcomplexes.
CC       {ECO:0000269|PubMed:24165940}.
CC   -!- SUBUNIT: Homodimer. Component of the autophagy-specific VPS34 PI3-
CC       kinase complex I composed of VPS15, VPS30, VPS34, ATG14 and ATG38.
CC       Interacts directly with ATG14 and VPS34. {ECO:0000269|PubMed:24165940}.
CC   -!- INTERACTION:
CC       Q05789; P38270: ATG14; NbExp=15; IntAct=EBI-35873, EBI-2699;
CC       Q05789; Q05789: ATG38; NbExp=3; IntAct=EBI-35873, EBI-35873;
CC       Q05789; P22543: VPS34; NbExp=5; IntAct=EBI-35873, EBI-20405;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC       Preautophagosomal structure membrane {ECO:0000269|PubMed:24165940};
CC       Peripheral membrane protein {ECO:0000305|PubMed:24165940}.
CC       Note=Localization to the preautophagosomal structure requires ATG14.
CC       {ECO:0000269|PubMed:24165940}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB67441.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; U14913; AAB67441.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BK006945; DAA09528.1; -; Genomic_DNA.
DR   PIR; S48562; S48562.
DR   RefSeq; NP_013312.2; NM_001182098.1.
DR   PDB; 5KC1; X-ray; 2.20 A; A/B/C/D/E/F/G/H/I/J/K/L=1-226.
DR   PDBsum; 5KC1; -.
DR   AlphaFoldDB; Q05789; -.
DR   SMR; Q05789; -.
DR   BioGRID; 31479; 34.
DR   ComplexPortal; CPX-1881; Phosphatidylinositol 3-kinase complex, class III, type I.
DR   DIP; DIP-4299N; -.
DR   IntAct; Q05789; 5.
DR   MINT; Q05789; -.
DR   STRING; 4932.YLR211C; -.
DR   iPTMnet; Q05789; -.
DR   MaxQB; Q05789; -.
DR   PaxDb; Q05789; -.
DR   PRIDE; Q05789; -.
DR   EnsemblFungi; YLR211C_mRNA; YLR211C; YLR211C.
DR   GeneID; 850908; -.
DR   KEGG; sce:YLR211C; -.
DR   SGD; S000004201; ATG38.
DR   VEuPathDB; FungiDB:YLR211C; -.
DR   eggNOG; ENOG502S4WG; Eukaryota.
DR   HOGENOM; CLU_107237_0_0_1; -.
DR   InParanoid; Q05789; -.
DR   OMA; NSEMKIN; -.
DR   BioCyc; YEAST:G3O-32328-MON; -.
DR   PRO; PR:Q05789; -.
DR   Proteomes; UP000002311; Chromosome XII.
DR   RNAct; Q05789; protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0000407; C:phagophore assembly site; IDA:SGD.
DR   GO; GO:0034045; C:phagophore assembly site membrane; IC:ComplexPortal.
DR   GO; GO:0034271; C:phosphatidylinositol 3-kinase complex, class III, type I; IDA:SGD.
DR   GO; GO:0005774; C:vacuolar membrane; IDA:SGD.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0005198; F:structural molecule activity; IMP:SGD.
DR   GO; GO:0006914; P:autophagy; IDA:ComplexPortal.
DR   GO; GO:0016236; P:macroautophagy; IMP:SGD.
DR   GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IC:ComplexPortal.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Autophagy; Coiled coil; Cytoplasm; Membrane;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   CHAIN           2..226
FT                   /note="Autophagy-related protein 38"
FT                   /id="PRO_0000203237"
FT   COILED          52..85
FT                   /evidence="ECO:0000255"
FT   COILED          161..215
FT                   /evidence="ECO:0000255"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   HELIX           125..127
FT                   /evidence="ECO:0007829|PDB:5KC1"
FT   HELIX           129..150
FT                   /evidence="ECO:0007829|PDB:5KC1"
FT   HELIX           156..160
FT                   /evidence="ECO:0007829|PDB:5KC1"
FT   HELIX           164..208
FT                   /evidence="ECO:0007829|PDB:5KC1"
SQ   SEQUENCE   226 AA;  25975 MW;  1F163DD0AE29B0F5 CRC64;
     MSTLAEVYTI IEDAEQECRK GDFTNAKAKY QEAIEVLGPQ NENLSQNKLS SDVTQAIDLL
     KQDITAKIQE LELLIEKQSS EENNIGMVNN NMLIGSVILN NKSPINGISN ARNWDNPAYQ
     DTLSPINDPL LMSILNRLQF NLNNDIQLKT EGGKNSKNSE MKINLRLEQF KKELVLYEQK
     KFKEYGMKID EITKENKKLA NEIGRLRERW DSLVESAKQR RDKQKN
 
 
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